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P58913 (CO16A_CONPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-conotoxin PVIA
Alternative name(s):
Lockjaw peptide
OrganismConus purpurascens (Purple cone)
Taxonomic identifier41690 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length81 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. In mice, injection of this toxin causes hyperactivity, rapid running, limb extension, and death. In fish, the peptide elicites spurts of rapid swimming, with twisted motions, quivering fins and the lockjaw extended mouth syndrome. Rigid paralysis and death are observed at higher doses. In mollusks, this peptide is inactive. Injection of this peptide together with the kappa-conotoxin PVIIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal "fin-pop" in envenomed fish.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom duct.

Domain

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin By similarity.

The cysteine framework is VI/VII (C-C-CC-C-C).

Post-translational modification

The difference between delta-conotoxin PVIA and [deamido]-delta-conotoxin PVIA lies in the state of amidation of Gly-80.

Sequence similarities

Belongs to the conotoxin O1 superfamily.

Mass spectrometry

Molecular mass is 2997.3 Da from positions 52 - 80. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4927 By similarity
PRO_0000034898
Peptide52 – 8029Delta-conotoxin PVIA Ref.1 Ref.2
PRO_0000034899

Amino acid modifications

Modified residue5714-hydroxyproline Ref.1
Modified residue6514-hydroxyproline Ref.1
Modified residue801Glycine amide; in form delta-conotoxin PVIA
Disulfide bond54 ↔ 69 By similarity
Disulfide bond61 ↔ 73 By similarity
Disulfide bond68 ↔ 78 By similarity

Experimental info

Mutagenesis591T → A: No loss of activity. Ref.3
Mutagenesis601F → A: Loss of biological activity. However, coinjection of this mutant protects against the wild-type conotoxin, suggesting that the mutant binds competitively to the wild-type conotoxin ligand site. Such a protective effect does not occur for all physiological targets. Ref.3
Mutagenesis631I → A: Loss of activity. Ref.3
Mutagenesis641K → A: No loss of activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P58913 [UniParc].

Last modified July 26, 2002. Version 1.
Checksum: ACCFE9E1C65ABFEC

FASTA818,945
        10         20         30         40         50         60 
MKLTCVMIVA VLFLTAWTFV TADDSKNGLE NHFWKARDEM KNREASKLDK KEACYAPGTF 

        70         80 
CGIKPGLCCS EFCLPGVCFG G 

« Hide

References

[1]"Purification, characterization, synthesis, and cloning of the lockjaw peptide from Conus purpurascens venom."
Shon K.-J., Grilley M.M., Marsh M., Yoshikami D., Hall A.R., Kurz B., Gray W.R., Imperial J.S., Hillyard D.R., Olivera B.M.
Biochemistry 34:4913-4918(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-80, SYNTHESIS OF 52-80, HYDROXYLATION AT PRO-57 AND PRO-65, MASS SPECTROMETRY.
Tissue: Venom and Venom duct.
[2]"Strategy for rapid immobilization of prey by a fish-hunting marine snail."
Terlau H., Shon K.-J., Grilley M.M., Stocker M., Stuehmer W., Olivera B.M.
Nature 381:148-151(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-80, SYNTHESIS OF 52-80.
[3]"Delta-conotoxin structure/function through a cladistic analysis."
Bulaj G., DeLaCruz R., Azimi-Zonooz A., West P., Watkins M., Yoshikami D., Olivera B.M.
Biochemistry 40:13201-13208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 52-80, MUTAGENESIS OF THR-59; PHE-60; ILE-63 AND LYS-64.

Cross-references

Sequence databases

PIRA58651.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer1563. PVIA precursor.

Family and domain databases

InterProIPR004214. Conotoxin.
IPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PfamPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCO16A_CONPU
AccessionPrimary (citable) accession number: P58913
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 26, 2002
Last modified: October 16, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families